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PMID: 194244 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Primary structure of very low density apolipoprotein C-II of human plasma.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 74 ·No. 5 ·1977-05-00 ·Pages 1942-5

Jackson RL, Baker HN, Gilliam EB, Gotto AM

Abstract

Apolipoprotein C-II (apoC-II), a protein constituent of very low density lipoproteins of human plasma and the activator protein of lipoprotein lipase, has been isolated and its amino acid sequence has been studied. The protein has 78 amino acid residues and is lacking cysteine, cystine, and histidine. Chromatography on Bio-Gel P-30 in 25% formic acid of the cyanogen bromide digest of apoC-II yields three fragments designated as CNBr-I, -II, and -III. They contained 50, 19, and 9 residues, respectively. The alignment of the cyanogen bromide fragments has been established as CNBr-III-I-II by isolation and sequence of the tryptic peptides of the intact protein. The amino acid sequences of the tryptic and CNBr peptides were determined by conventional methods. With this information, it was possible to establish the complete amino acid sequence of apoC-II.

MeSH Terms
Amino Acid Sequence Apolipoproteins/blood,isolation & purification Cyanogen Bromide Humans Lipoproteins, VLDL/blood Trypsin/metabolism
Chemicals
Apolipoproteins Lipoproteins, VLDL Trypsin Cyanogen Bromide
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Jackson R L
Baker H N
Gilliam E B
Gotto A M
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30 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.74.5.1942
Published
1977-05-00
Pages
1942-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC431048
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.74.5.1942 PMC Full Text View journal details
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